The antibody AK4 recognizes an extracellular epitope of CD62P (P-selectin), a 140 kD single chain type I transmembrane glycoprotein present in secretory alpha-granules in platelets, in Weibel-Palade bodies in endothelial cells and in megakaryocytes, it is relocated to the plasma membrane upon activation.
Cross-Reactivity (Details)
Human, Non-Human Primates
Purification
Purified by protein-A affinity chromatography.
Purity
> 95 % (by SDS-PAGE)
Endotoxin Level
Endotoxin level is less than 0.01 EU/µg of the protein, as determined by the LAL test.
Kowalska, Ratajczak, Hoxie, Brass, Gewirtz, Poncz, Ratajczak: "Megakaryocyte precursors, megakaryocytes and platelets express the HIV co-receptor CXCR4 on their surface: determination of response to stromal-derived factor-1 by megakaryocytes and platelets." in: British journal of haematology, Vol. 104, Issue 2, pp. 220-9, (1999) (PubMed).
Dunlop, Skinner, Bendall, Favaloro, Castaldi, Gorman, Gamble, Vadas, Berndt: "Characterization of GMP-140 (P-selectin) as a circulating plasma protein." in: The Journal of experimental medicine, Vol. 175, Issue 4, pp. 1147-50, (1992) (PubMed).
Target
P-Selectin (SELP)
(Selectin P (Granule Membrane Protein 140kDa, Antigen CD62) (SELP))
Selectin P,CD62P (P-selectin) is an adhesion glycoprotein that is expressed on platelets and endothelial cells upon their activation. Interaction between CD62P and its mucin-like ligand PSGL-1 (P-selectin glycoprotein ligand-1) expressed on the microvilli of most leukocytes supports leukocyte rolling along postkapillary venules at the earliest time of inflammation. Both CD62P and PSGL-1 are extended glycoproteins that form homodimers. CD62P dimerization is probably mediated through interactions of the transmembrane domains and stabilizes leukocyte tethering and rolling, probably by increasing rebinding within a bond cluster.,P-selectin, GMP140, SELP, PADGEM, GRMP, LECAM3, PSEL